3EB6
Structure of the cIAP2 RING domain bound to UbcH5b
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0016740 | molecular_function | transferase activity |
| B | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| B | 0070936 | biological_process | protein K48-linked ubiquitination |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS557 |
| A | CYS560 |
| A | CYS578 |
| A | CYS581 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | CYS572 |
| A | HIS574 |
| A | CYS588 |
| A | CYS591 |
Functional Information from PROSITE/UniProt
| site_id | PS00183 |
| Number of Residues | 16 |
| Details | UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL |
| Chain | Residue | Details |
| B | TYR74-LEU89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 146 |
| Details | Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






